1g8x
From Proteopedia
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STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR
Overview
Molecular motors move unidirectionally along polymer tracks, producing, movement and force in an ATP-dependent fashion. They achieve this by, amplifying small conformational changes in the nucleotide-binding region, into force-generating movements of larger protein domains. We present the, 2.8 A resolution crystal structure of an artificial actin-based motor. By, combining the catalytic domain of myosin II with a 130 A conformational, amplifier consisting of repeats 1 and 2 of alpha-actinin, we demonstrate, that it is possible to genetically engineer single-polypeptide molecular, motors with precisely defined lever arm lengths and specific motile, properties. Furthermore, our structure shows the consequences of mutating, a conserved salt bridge in the nucleotide-binding region. Disruption of, this salt bridge, which is known to severely inhibit ATP hydrolysis, activity, appears to interfere with formation of myosin's catalytically, active 'closed' conformation. Finally, we describe the structure of, alpha-actinin repeats 1 and 2 as being composed of two rigid, triple-helical bundles linked by an uninterrupted alpha-helix. This fold, is very similar to the previously described structures of alpha-actinin, repeats 2 and 3, and alpha-spectrin repeats 16 and 17.
About this Structure
1G8X is a Single protein structure of sequence from Dictyostelium discoideum with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a genetically engineered molecular motor., Kliche W, Fujita-Becker S, Kollmar M, Manstein DJ, Kull FJ, EMBO J. 2001 Jan 15;20(1-2):40-6. PMID:11226153
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